Abstract:
:A structure of residues 1-177 of the cyclophilin domain of a large divergent cyclophilin from the filarial nematode parasite Brugia malayi has been crystallised and solved in two different crystal forms. The active site has a similar structure to that of human cyclophilin A. Two of the 13 residues important in forming the human cyclophilin A/cyclosporin A complex are altered in the B. malayi cyclophilin and explain the relatively poor inhibition of peptidyl prolyl isomerase activity by cyclosporin A.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Taylor P,Page AP,Kontopidis G,Husi H,Walkinshaw MDdoi
10.1016/s0014-5793(98)00264-6subject
Has Abstractpub_date
1998-03-27 00:00:00pages
361-6issue
2eissn
0014-5793issn
1873-3468pii
S0014-5793(98)00264-6journal_volume
425pub_type
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